Curated Information
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Curated Information Page
PubMed Id: 16024771 
Tcherkezian J, et al. (2005) Extracellular signal-regulated kinase 1 interacts with and phosphorylates CdGAP at an important regulatory site. Mol Cell Biol 25, 6314-29 16024771
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
Click on the protein name to open the protein page, and on the RSD number to open the site page.
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T769-p - CdGAP (mouse)
Orthologous residues
CdGAP (human): P782‑p, CdGAP (mouse): T769‑p, CdGAP (rat): P772‑p
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK1 (human)

T776-p - CdGAP (mouse)
Orthologous residues
CdGAP (human): T789‑p, CdGAP (mouse): T776‑p, CdGAP (rat): T779‑p
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, phosphoamino acid analysis, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  COS (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  monkey
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK1 (human) co-immunoprecipitation, pharmacological activator of upstream enzyme, modification site within consensus motif, pharmacological inhibitor of upstream enzyme
Downstream Regulation
 Effect of modification (function):  activity, inhibited
 Comments:  T776A mutant proteins have increased GAP activity toward Rac1 in response to RasV12 signaling.

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